Structural mannoproteins released by beta-elimination from Candida albicans cell walls

FEMS Microbiol Lett. 1994 Oct 15;123(1-2):131-6. doi: 10.1111/j.1574-6968.1994.tb07212.x.


Mild alkaline solutions (beta-elimination), after removing the non-covalently bonded wall materials by hot SDS, released 13% and 26% of remaining wall proteins from mycelial and yeast cells of Candida albicans, respectively. When the beta-elimination was carried out after digestion of the walls with chitinase, four-fold more proteinaceous materials were released from mycelium and a similar amount in yeast walls. The solubilized materials were shown to be highly polydisperse, and endo-glycosidase H reduced their polydispersity and molecular masses, revealing different electrophoretic patterns in yeast and mycelial cell walls. The solubilized mycelial proteins carried N-glycosidic sugar chains and the epitopes recognized by two monoclonal antibodies were preserved, although showing a different behaviour in yeast walls. These results are consistent with the idea that significant amounts of intrinsic O-glycosylated mannoproteins are interconnected in the walls of C. albicans.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Antibodies, Monoclonal
  • Candida albicans / chemistry*
  • Cell Wall / chemistry*
  • Chitinases / chemistry
  • Hydrogen-Ion Concentration
  • Hydrolases / chemistry
  • Membrane Glycoproteins / immunology
  • Membrane Glycoproteins / isolation & purification*
  • Protein Hydrolysates / chemistry


  • Antibodies, Monoclonal
  • Membrane Glycoproteins
  • Protein Hydrolysates
  • mannoproteins
  • zymolyase
  • Hydrolases
  • Chitinases